CSF3_BOVIN
ID CSF3_BOVIN Reviewed; 195 AA.
AC P35833; Q9TV89;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Granulocyte colony-stimulating factor;
DE Short=G-CSF;
DE Flags: Precursor;
GN Name=CSF3; Synonyms=GCSF;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Holstein;
RX PubMed=10690933; DOI=10.1016/s0165-2427(99)00164-6;
RA Heidari M., Kehrli M.E. Jr.;
RT "Cloning, sequencing, and analysis of cDNA encoding bovine granulocyte-
RT colony stimulating factor.";
RL Vet. Immunol. Immunopathol. 73:183-191(2000).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RX PubMed=7504736; DOI=10.1006/jmbi.1993.1617;
RA Lovejoy B., Cascio D., Eisenberg D.;
RT "Crystal structure of canine and bovine granulocyte-colony stimulating
RT factor (G-CSF).";
RL J. Mol. Biol. 234:640-653(1993).
CC -!- FUNCTION: Granulocyte/macrophage colony-stimulating factors are
CC cytokines that act in hematopoiesis by controlling the production,
CC differentiation, and function of 2 related white cell populations of
CC the blood, the granulocytes and the monocytes-macrophages. This CSF
CC induces granulocytes.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- PTM: O-glycosylated.
CC -!- SIMILARITY: Belongs to the IL-6 superfamily. {ECO:0000305}.
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DR EMBL; AF092533; AAD16102.1; -; mRNA.
DR RefSeq; NP_776453.1; NM_174028.1.
DR PDB; 1BGC; X-ray; 1.70 A; A=22-195.
DR PDBsum; 1BGC; -.
DR AlphaFoldDB; P35833; -.
DR SMR; P35833; -.
DR STRING; 9913.ENSBTAP00000028610; -.
DR PaxDb; P35833; -.
DR Ensembl; ENSBTAT00000028610; ENSBTAP00000028610; ENSBTAG00000021462.
DR GeneID; 281096; -.
DR KEGG; bta:281096; -.
DR CTD; 1440; -.
DR VEuPathDB; HostDB:ENSBTAG00000021462; -.
DR VGNC; VGNC:27757; CSF3.
DR eggNOG; ENOG502SCNA; Eukaryota.
DR GeneTree; ENSGT00390000017328; -.
DR HOGENOM; CLU_118367_0_0_1; -.
DR InParanoid; P35833; -.
DR OMA; HHQVGGF; -.
DR OrthoDB; 1289639at2759; -.
DR TreeFam; TF337698; -.
DR Reactome; R-BTA-9705462; Inactivation of CSF3 (G-CSF) signaling.
DR EvolutionaryTrace; P35833; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000021462; Expressed in intramuscular adipose tissue and 55 other tissues.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
DR GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
DR GO; GO:0005130; F:granulocyte colony-stimulating factor receptor binding; IBA:GO_Central.
DR GO; GO:0008083; F:growth factor activity; IBA:GO_Central.
DR GO; GO:0071345; P:cellular response to cytokine stimulus; IEA:Ensembl.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
DR GO; GO:2000251; P:positive regulation of actin cytoskeleton reorganization; IEA:Ensembl.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IEA:Ensembl.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IBA:GO_Central.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IEA:Ensembl.
DR GO; GO:0045639; P:positive regulation of myeloid cell differentiation; IBA:GO_Central.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IEA:Ensembl.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IEA:Ensembl.
DR GO; GO:0032092; P:positive regulation of protein binding; IEA:Ensembl.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR Gene3D; 1.20.1250.10; -; 1.
DR InterPro; IPR009079; 4_helix_cytokine-like_core.
DR InterPro; IPR040117; GCSF/MGF.
DR InterPro; IPR030474; IL-6/GCSF/MGF.
DR InterPro; IPR030473; IL6/GCSF/MGF_CS.
DR PANTHER; PTHR10511; PTHR10511; 1.
DR Pfam; PF16647; GCSF; 1.
DR PIRSF; PIRSF001935; IL6_MGF_GCSF; 1.
DR PRINTS; PR00433; IL6GCSFMGF.
DR SMART; SM00126; IL6; 1.
DR SUPFAM; SSF47266; SSF47266; 1.
DR PROSITE; PS00254; INTERLEUKIN_6; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytokine; Disulfide bond; Glycoprotein; Growth factor;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..195
FT /note="Granulocyte colony-stimulating factor"
FT /id="PRO_0000015568"
FT CARBOHYD 154
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
FT DISULFID 57..63
FT DISULFID 85..95
FT CONFLICT 93..94
FT /note="TS -> RG (in Ref. 2)"
FT /evidence="ECO:0000305"
FT HELIX 32..60
FT /evidence="ECO:0007829|PDB:1BGC"
FT HELIX 65..69
FT /evidence="ECO:0007829|PDB:1BGC"
FT HELIX 72..75
FT /evidence="ECO:0007829|PDB:1BGC"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:1BGC"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:1BGC"
FT HELIX 92..112
FT /evidence="ECO:0007829|PDB:1BGC"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:1BGC"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:1BGC"
FT HELIX 121..145
FT /evidence="ECO:0007829|PDB:1BGC"
FT HELIX 164..191
FT /evidence="ECO:0007829|PDB:1BGC"
SQ SEQUENCE 195 AA; 21431 MW; 8C06119E4ADFBA73 CRC64;
MKLMVLQLLL WHSALWTVHE ATPLGPARSL PQSFLLKCLE QVRKIQADGA ELQERLCAAH
KLCHPEELML LRHSLGIPQA PLSSCSSQSL QLTSCLNQLH GGLFLYQGLL QALAGISPEL
APTLDTLQLD VTDFATNIWL QMEDLGAAPA VQPTQGAMPT FTSAFQRRAG GVLVASQLHR
FLELAYRGLR YLAEP
